- match to AD106_G4_424 (42% id) - no match in both acidobacterial genomes - environment conserved in clones? - to be verified

LUAcid_AD55_D2_29

39888

37786

quinoprotein glucose dehydrogenase

1

R

ADDED

- best match to quinate/shikimate dehydrogenase, putative marine gamma proteobacterium HTCC2143 (41% id) - orthologs affiliated to proteobacteria and few other bacteria - IPR011047 Quinonprotein alcohol dehydrogenase-like: Quinoprotein alcohol dehydrogenases are a family of proteins found in methylotrophic or autotrophic bacteria - large family in B, A and E

PROTEIN

COG4993 Glucose dehydrogenase

G Carbohydrate transport and metabolism

Good

B

82.227.62.180

26/09/07 08:08:48

- several matches to Solibacter (best 42% id), not to Ellin345 strain - high number of matches in Solibacter, but only some in other bacterial genomes - match to KM3_25_B4_257 and KM3_25_B4_153 - environment conserved? - to be verified

- several matches to acidobacteria clones - one matche to each Solibacter and Ellin345 - environment conserved? - to be verified

LUAcid_AD55_D2_16

24201

23215

Alcohol dehydrogenase GroES domain protein

1

R

ADDED

- IPR002085 family Alcohol dehydrogenase superfamily, zinc-containing - best match Archaea - best match to Alcohol dehydrogenase GroES domain protein Candidatus Nitrosopumilus maritimus SCM1 (50% id) - GroES (chaperonin 10) is an oligomeric molecular chaperone, which functions in protein folding and possibly in intercellular signalling, being found on the surface of various prokaryotic and eukaryotic cells, as well as being released from cells - high of domains found also in E

- environment conserved in Acidobacteria - also in soil clones - to be verified

LUAcid_AD55_D2_08

7804

8514

phosphoribosylformylglycinamidine synthase I (PurQ)

1

D

ADDED

6.3.5.3

- purin biosynthesis operon - IPR010075 Phosphoribosylformylglycinamidine synthase I - In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This entry describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea.

- environment conserved in Acidobacteria - also in soil clones - to be verified

LUAcid_AD55_D2_07

7568

7804

phosphoribosylformylglycinamidine synthase I (PurS component)

1

D

ADDED

6.3.5.3

- purin biosynthesis operon IPR003850 Phosphoribosylformylglycinamidine synthetase PurS Therefore, the PurS protein appears to be required for the function of the PurL and PurQ subunits of the FGAM synthetase, but the molecular mechanism for the functional role of PurS is currently not known